dbPTM

NMT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NMT1_HUMAN
UniProt AC	P30419
Protein Name	Glycylpeptide N-tetradecanoyltransferase 1
Gene Name	NMT1
Organism	Homo sapiens (Human).
Sequence Length	496
Subcellular Localization	Cytoplasm . Cytoplasm, cytosol . Membrane Peripheral membrane protein . Copurifies with ribosomes.
Protein Description	Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins..
Protein Sequence	MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKKQKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MADESETAVKPP ---CCCCCCCCCCCC	40.57	26074081
7	Phosphorylation	-MADESETAVKPPAP -CCCCCCCCCCCCCC	46.13	23663014
14 (in isoform 2)	Ubiquitination	-	36.41	21890473
31	Phosphorylation	GNGHEHCSDCENEED CCCCCCCCCCCCCCC	47.40	23401153
40	Phosphorylation	CENEEDNSYNRGGLS CCCCCCCCCCCCCCC	35.79	23663014
41	Phosphorylation	ENEEDNSYNRGGLSP CCCCCCCCCCCCCCC	18.35	23663014
47	Phosphorylation	SYNRGGLSPANDTGA CCCCCCCCCCCCCCH	25.82	29255136
52	Phosphorylation	GLSPANDTGAKKKKK CCCCCCCCCHHHHHH	38.56	23927012
55	2-Hydroxyisobutyrylation	PANDTGAKKKKKKQK CCCCCCHHHHHHHHH	67.48	-
55	Acetylation	PANDTGAKKKKKKQK CCCCCCHHHHHHHHH	67.48	25953088
55	Ubiquitination	PANDTGAKKKKKKQK CCCCCCHHHHHHHHH	67.48	29967540
56	Acetylation	ANDTGAKKKKKKQKK CCCCCHHHHHHHHHH	70.10	25953088
69	Phosphorylation	KKKKEKGSETDSAQD HHHHHCCCCCCCCCC	48.68	29255136
71	Phosphorylation	KKEKGSETDSAQDQP HHHCCCCCCCCCCCC	36.63	29255136
73	Phosphorylation	EKGSETDSAQDQPVK HCCCCCCCCCCCCCC	34.94	29255136
80	Ubiquitination	SAQDQPVKMNSLPAE CCCCCCCCCCCCCHH	38.76	21906983
80 (in isoform 1)	Ubiquitination	-	38.76	21890473
83	Phosphorylation	DQPVKMNSLPAERIQ CCCCCCCCCCHHHHH	32.03	30266825
94 (in isoform 1)	Ubiquitination	-	57.92	21890473
94	Ubiquitination	ERIQEIQKAIELFSV HHHHHHHHHHHHHCC	57.92	23000965
100	Phosphorylation	QKAIELFSVGQGPAK HHHHHHHCCCCCCCC	37.65	28555341
116	Phosphorylation	MEEASKRSYQFWDTQ HHHHHHHHHCCCCCC	27.33	21945579
117	Phosphorylation	EEASKRSYQFWDTQP HHHHHHHHCCCCCCC	16.26	21945579
127	Ubiquitination	WDTQPVPKLGEVVNT CCCCCCCCCCCCCCC	70.16	29967540
142	Acetylation	HGPVEPDKDNIRQEP CCCCCCCCCCCCCCC	64.49	25953088
142	Ubiquitination	HGPVEPDKDNIRQEP CCCCCCCCCCCCCCC	64.49	29967540
180	Phosphorylation	YTLLNENYVEDDDNM HHHHHHCCCCCCCCC	10.07	22817900
187	Sulfoxidation	YVEDDDNMFRFDYSP CCCCCCCCEEECCCH	3.07	30846556
227	Phosphorylation	RKLVGFISAIPANIH CHHHHHHEEECCCEE	20.20	21406692
236	Phosphorylation	IPANIHIYDTEKKMV ECCCEEEEECCCCEE	11.58	21406692
238	Phosphorylation	ANIHIYDTEKKMVEI CCEEEEECCCCEEEE	32.50	21406692
240	Acetylation	IHIYDTEKKMVEINF EEEEECCCCEEEEEE	48.54	26051181
281	Phosphorylation	EGIFQAVYTAGVVLP HHHHHHHHEECEECC	8.22	-
300	Phosphorylation	TCRYWHRSLNPRKLI CCHHHHHCCCHHHEE	21.44	27251275
310	Ubiquitination	PRKLIEVKFSHLSRN HHHEEEEECHHHCCC	28.49	33845483
310	Acetylation	PRKLIEVKFSHLSRN HHHEEEEECHHHCCC	28.49	26051181
319	Phosphorylation	SHLSRNMTMQRTMKL HHHCCCCCHHHHHHH	17.44	23312004
323	Phosphorylation	RNMTMQRTMKLYRLP CCCCHHHHHHHHCCC	11.19	25219547
325	Ubiquitination	MTMQRTMKLYRLPET CCHHHHHHHHCCCCC	41.58	-
327	Phosphorylation	MQRTMKLYRLPETPK HHHHHHHHCCCCCCC	12.46	25219547
332	Phosphorylation	KLYRLPETPKTAGLR HHHCCCCCCCCCCCC	28.31	25219547
334	Ubiquitination	YRLPETPKTAGLRPM HCCCCCCCCCCCCCC	59.43	29967540
343	Phosphorylation	AGLRPMETKDIPVVH CCCCCCCCCCCHHHH	27.97	21406692
420	Phosphorylation	HKSLKAAYSFYNVHT HHHHHHHHHHHCCCC	12.27	28270605
421	Phosphorylation	KSLKAAYSFYNVHTQ HHHHHHHHHHCCCCC	19.27	28270605
423	Phosphorylation	LKAAYSFYNVHTQTP HHHHHHHHCCCCCCH	15.44	28270605
427	Phosphorylation	YSFYNVHTQTPLLDL HHHHCCCCCCHHHHH	29.83	28270605
429	Phosphorylation	FYNVHTQTPLLDLMS HHCCCCCCHHHHHHH	19.63	28270605
436	Phosphorylation	TPLLDLMSDALVLAK CHHHHHHHHHHHHHH	27.33	28270605
445	2-Hydroxyisobutyrylation	ALVLAKMKGFDVFNA HHHHHHHCCCCHHHH	56.57	-
445	Ubiquitination	ALVLAKMKGFDVFNA HHHHHHHCCCCHHHH	56.57	-
459	Ubiquitination	ALDLMENKTFLEKLK HHHHHCCHHHHHHHC	27.61	29967540
464	2-Hydroxyisobutyrylation	ENKTFLEKLKFGIGD CCHHHHHHHCCCCCC	60.15	-
464	Ubiquitination	ENKTFLEKLKFGIGD CCHHHHHHHCCCCCC	60.15	-
482	Ubiquitination	QYYLYNWKCPSMGAE EEEEEECCCCCCCCC	32.41	21963094

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
37	Y	Phosphorylation	Kinase	LYN	P07948	GPS
70	Y	Phosphorylation	Kinase	LYN	P07948	GPS
93	Y	Phosphorylation	Kinase	LYN	P07948	GPS
100	Y	Phosphorylation	Kinase	FYN	P06241	GPS
117	Y	Phosphorylation	Kinase	LYN	P07948	PhosphoELM
180	Y	Phosphorylation	Kinase	FYN	P06241	PSP
180	Y	Phosphorylation	Kinase	LYN	P07948	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NMT1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NMT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CABP2_HUMAN	CABP2	physical	10625670
CABP1_HUMAN	CABP1	physical	10625670
GAG_HV1H2	gag	physical	16501079
HNRPM_HUMAN	HNRNPM	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
ILF2_HUMAN	ILF2	physical	22863883
MTAP2_HUMAN	MAP2	physical	22863883
MRE11_HUMAN	MRE11A	physical	22863883
PDCD6_HUMAN	PDCD6	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
CAN1_HUMAN	CAPN1	physical	16530191
P53_HUMAN	TP53	physical	16530191
ACSL4_HUMAN	ACSL4	physical	26344197
DJC13_HUMAN	DNAJC13	physical	27173435
EDRF1_HUMAN	EDRF1	physical	27173435
FYB2_HUMAN	C1orf168	physical	27173435
I2BP1_HUMAN	IRF2BP1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NMT1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	17081983 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	15302935 [Abstract]